IMP-51, a Novel IMP-Type Metallo-β-Lactamase with Increased Doripenem- and Meropenem-Hydrolyzing Activities, in a Carbapenem-Resistant Pseudomonas aeruginosa Clinical Isolate | Zendy

Tatsuya Tada | Zendy; Pham Hong Nhung | Zendy; Tohru MiyoshiAkiyama | Zendy; Kayo Shimada | Zendy; Doan Mai Phuong | Zendy; Nguyen Quoc Anh | Zendy; Norio Ohmagari | Zendy; Teruo Kirikae | Zendy

Open Access

IMP-51, a Novel IMP-Type Metallo-β-Lactamase with Increased Doripenem- and Meropenem-Hydrolyzing Activities, in a Carbapenem-Resistant Pseudomonas aeruginosa Clinical Isolate

Author(s) -

Tatsuya Tada,

Pham Hong Nhung,

Tohru MiyoshiAkiyama,

Kayo Shimada,

Doan Mai Phuong,

Nguyen Quoc Anh,

Norio Ohmagari,

Teruo Kirikae

Publication year - 2015

Publication title -

antimicrobial agents and chemotherapy

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 2.07

H-Index - 259

eISSN - 1070-6283

pISSN - 0066-4804

DOI - 10.1128/aac.01611-15

Subject(s) - meropenem , doripenem , cefoxitin , microbiology and biotechnology , pseudomonas aeruginosa , carbapenem , escherichia coli , biology , bacteria , biochemistry , antibiotic resistance , antibiotics , gene , genetics , staphylococcus aureus

A meropenem-resistantPseudomonas aeruginosa isolate was obtained from a patient in a medical setting in Hanoi, Vietnam. The isolate was found to have a novel IMP-type metallo-β-lactamase, IMP-51, which differed from IMP-7 by an amino acid substitution (Ser262Gly).Escherichia coli expressingbla IMP-51 showed greater resistance to cefoxitin, meropenem, and moxalactam thanE. coli expressingbla IMP-7 . The amino acid residue at position 262 was located near the active site, proximal to the H263 Zn(II) ligand.

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